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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/FKB39_DROME FKB39_DROME]] PPIases accelerate the folding of proteins. May function in a signal transduction cascade during early development. | [[http://www.uniprot.org/uniprot/FKB39_DROME FKB39_DROME]] PPIases accelerate the folding of proteins. May function in a signal transduction cascade during early development. | ||
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== Publication Abstract from PubMed == | |||
Nucleoplasmin is a histone chaperone that consists of a pentameric N-terminal domain and an unstructured C-terminal tail. The pentameric core domain, a doughnut-like structure with a central pore, is only found in the nucleoplasmin family. Here, we report the first structure of a nucleoplasmin-like domain (NPL) from the unrelated Drosophila protein, FKBP39, and we present evidence that this protein associates with chromatin. Furthermore, we show that two other chromatin proteins, Arabidopsis thaliana histone deacetylase type 2 (HD2) and Saccharomyces cerevisiae Fpr4, share the NPL fold and form pentamers, or a dimer of pentamers in the case of HD2. Thus, we propose a new family of proteins that share the pentameric nucleoplasmin-like NPL domain and are found in protists, fungi, plants and animals. | |||
The Pentameric Nucleoplasmin Fold Is Present in Drosophila FKBP39 and a Large Number of Chromatin-Related Proteins.,Edlich-Muth C, Artero JB, Callow P, Przewloka MR, Watson AA, Zhang W, Glover DM, Debski J, Dadlez M, Round AR, Forsyth VT, Laue ED J Mol Biol. 2015 Mar 24. pii: S0022-2836(15)00194-1. doi:, 10.1016/j.jmb.2015.03.010. PMID:25813344<ref>PMID:25813344</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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==See Also== | |||
*[[FK506 binding protein|FK506 binding protein]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 09:45, 15 April 2015
Structure of the Nucleoplasmin-like N-terminal domain of Drosophila FKBP39Structure of the Nucleoplasmin-like N-terminal domain of Drosophila FKBP39
Structural highlights
Function[FKB39_DROME] PPIases accelerate the folding of proteins. May function in a signal transduction cascade during early development. Publication Abstract from PubMedNucleoplasmin is a histone chaperone that consists of a pentameric N-terminal domain and an unstructured C-terminal tail. The pentameric core domain, a doughnut-like structure with a central pore, is only found in the nucleoplasmin family. Here, we report the first structure of a nucleoplasmin-like domain (NPL) from the unrelated Drosophila protein, FKBP39, and we present evidence that this protein associates with chromatin. Furthermore, we show that two other chromatin proteins, Arabidopsis thaliana histone deacetylase type 2 (HD2) and Saccharomyces cerevisiae Fpr4, share the NPL fold and form pentamers, or a dimer of pentamers in the case of HD2. Thus, we propose a new family of proteins that share the pentameric nucleoplasmin-like NPL domain and are found in protists, fungi, plants and animals. The Pentameric Nucleoplasmin Fold Is Present in Drosophila FKBP39 and a Large Number of Chromatin-Related Proteins.,Edlich-Muth C, Artero JB, Callow P, Przewloka MR, Watson AA, Zhang W, Glover DM, Debski J, Dadlez M, Round AR, Forsyth VT, Laue ED J Mol Biol. 2015 Mar 24. pii: S0022-2836(15)00194-1. doi:, 10.1016/j.jmb.2015.03.010. PMID:25813344[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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